Evidence map›Paper›PMID 32586350›Full record

ArticleBMC genomics2020

Protein acetylation in mitochondria plays critical functions in the pathogenesis of fatty liver disease.

Zhang Le-Tian, Hu Cheng-Zhang, Zhang Xuan, Qin Zhang, Yan Zhen-Gui, Wei Qing-Qing, Wang Sheng-Xuan, Xu Zhong-Jin, Li Ran-Ran, Liu Ting-Jun and 3 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC genomics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.9field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 46 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 1 institution in 1 country.

Zhang Le-TianShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Hu Cheng-ZhangShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Zhang XuanShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Qin ZhangShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Yan Zhen-GuiShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Wei Qing-QingShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Wang Sheng-XuanShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Xu Zhong-JinShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Li Ran-RanShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Liu Ting-JunShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Su Zhong-QuShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Wang Zhong-HuaShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China.
Shi Ke-RongShandong Key Laboratory of Animal Bioengineering and Disease Prevention, College of Animal Science and Technology, Shandong Agricultural University, No. 61 Daizong Street, Taian, Shandong, 271018, P. R. China. krshi@sdau.edu.cn.ORCID http://orcid.org/0000-0003-1966-7473
Shandong Agricultural University · CN

Funding

Key Project of Agricultural Fine Breeding of Shandong Province 2019LZGC011; 2016LZGC030National Natural Science Foundation of China 31402054Natural Science Foundation of Shandong Province ZR2013CM013
6 · The paper itself

Abstract

backgroundFatty liver is a high incidence of perinatal disease in dairy cows caused by negative energy balance, which seriously threatens the postpartum health and milk production. It has been reported that lysine acetylation plays an important role in substance and energy metabolism. Predictably, most metabolic processes in the liver, as a vital metabolic organ, are subjected to acetylation. Comparative acetylome study were used to quantify the hepatic tissues from the severe fatty liver group and normal group. Combined with bioinformatics analysis, this study provides new insights for the role of acetylation modification in fatty liver disease of dairy cows.

resultsWe identified 1841 differential acetylation sites on 665 proteins. Among of them, 1072 sites on 393 proteins were quantified. Functional enrichment analysis shows that higher acetylated proteins are significantly enriched in energy metabolic pathways, while lower acetylated proteins are significantly enriched in pathways related to immune response, such as drug metabolism and cancer. Among significantly acetylated proteins, many mitochondrial proteins were identified to be interacting with multiple proteins and involving in lipid metabolism. Furthermore, this study identified potential important proteins, such as HADHA, ACAT1, and EHHADH, which may be important regulatory factors through modification of acetylation in the development of fatty liver disease in dairy cows and possible therapeutic targets for NAFLD in human beings.

conclusionThis study provided a comprehensive acetylome profile of fatty liver of dairy cows, and revealed important biological pathways associated with protein acetylation occurred in mitochondria, which were involved in the regulation of the pathogenesis of fatty liver disease. Furthermore, potential important proteins, such as HADHA, ACAT1, EHHADH, were predicted to be essential regulators during the pathogenesis of fatty liver disease. The work would contribute to the understanding the pathogenesis of NAFLD, and inspire in the development of new therapeutic strategies for NAFLD.

Indexed as

AcetylationAnimalsCase-Control StudiesCattleCattle DiseasesChromatography, LiquidComputational BiologyEnergy MetabolismFatty LiverFemaleLipid MetabolismMitochondria, LiverMitochondrial ProteinsProtein Interaction MapsProteomicsTandem Mass SpectrometryMitochondrial ProteinsAcetylomeDairy cattleFatty liverLipid metabolismPerinatal period

Identifiers

PMID32586350
PMCPMC7318365
OpenAlexW3037616464

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.